Smad mediates BMP-2-induced upregulation of FGF-evoked PC12 cell differentiation |
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Authors: | Hayashi Hisaki Ishisaki Akira Imamura Toru |
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Affiliation: | Age Dimension Research Center, National Institute of Advanced Industrial Science and Technology, Tsukuba, Ibaraki 305-8566, Japan. |
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Abstract: | To gain insight into presenilin-1 (PS1) structural aspects, we explored the structure–function relationship of its N- and C-terminal (NTF and CTF, respectively) complexes. We demonstrated that both NTF and CTF act as independent but inter-changing binding units capable of binding each other (NTF/CTF) or their homologues (NTF/NTF; CTF/CTF). The Alzheimer’s disease-associated PS1 mutations Y115H and M146L do not affect their ability to hetero- and/or homodimerize, thus conserving their basic integrity and function(s). These results suggest that PS1 associates intra-molecularly to form higher order complexes, which may be needed for endoproteolytic cleavage and/or γ-secretase-associated activity. |
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Keywords: | Presenilin γ-secretase Homodimerization Heterodimerization |
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